Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Masazumi Matsumura"'
Autor:
Yatin R. Gokarn, Stephen R. Brych, Riki Stevenson, Rahul S. Rajan, Masazumi Matsumura, Heather Hultgen
Publikováno v:
Journal of Pharmaceutical Sciences. 99:764-781
Proteins are susceptible to degradation upon exposure to a variety of stresses during product manufacturing, transportation and storage. In this study, we investigated the aggregation properties of a monoclonal antibody during agitation stress. Agita
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2c49150be818ed5b963d84b6169ede8
https://doi.org/10.1002/jps.21868
https://doi.org/10.1002/jps.21868
Publikováno v:
Journal of Pharmaceutical Sciences. 98:3013-3030
Two major aggregation pathways observed in an IgG2 molecule are described. Different aggregate species generated by long-term incubation of the antibody at 37°C were collected by a semi-preparative size exclusion chromatography method. These purifie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a236eefd1613665cdf583bb888b4a354
https://doi.org/10.1002/jps.21514
https://doi.org/10.1002/jps.21514
Autor:
Louisa Vardanyan, Natalie Perico, Arnold McAuley, Douglas Rehder, Pavel V. Bondarenko, Jill Crouse-Zeineddini, David N. Brems, Thomas M. Dillon, Dirk Chelius, Venkat Mukku, Gang Xiao, Masazumi Matsumura
Publikováno v:
Biochemistry. 47:2518-2530
A new isoform of the light chain of a fully human monoclonal immunoglobulin gamma2 (IgG2) antibody panitumumab against human epidermal growth factor receptor (EGFR) was generated by in vitro aging. The isoform was attributed to the isomerization of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff6063aa9bd1edf62d612e9b169c3cea
https://doi.org/10.1021/bi7018223
https://doi.org/10.1021/bi7018223
Autor:
Carl G. Kolvenbach, Arnold McAuley, David N. Brems, Stephen R. Brych, Jaby Jacob, Kimberly Westland, Masazumi Matsumura, Hyo Jin Lee, Gerd R. Kleemann, Douglas Rehder
Publikováno v:
Protein Science. 17:95-106
Recombinant human monoclonal antibodies have become important protein-based therapeutics for the treatment of various diseases. The antibody structure is complex, consisting of beta-sheet rich domains stabilized by multiple disulfide bridges. The dim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d3a38b08695c29baa24c9574e4d6288
https://doi.org/10.1110/ps.073134408
https://doi.org/10.1110/ps.073134408
Autor:
Yoshikazu Imanishi, Peter S. Nelson, Geeng Fu Jang, Masazumi Matsumura, Krzysztof Palczewski, C.A.G.G. Driessen, Françoise Haeseleer
Publikováno v:
Journal of Biological Chemistry, 277, 45537-46
Journal of Biological Chemistry, 277, 47, pp. 45537-46
Journal of Biological Chemistry, 277, 47, pp. 45537-46
Contains fulltext : 185315.pdf (Publisher’s version ) (Open Access) Retinoids are chromophores involved in vision, transcriptional regulation, and cellular differentiation. Members of the short chain alcohol dehydrogenase/reductase superfamily cata
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::155628a29d024e315c2738c107403c75
https://doi.org/10.1074/jbc.m208882200
https://doi.org/10.1074/jbc.m208882200
Autor:
Olga V. Chumakova, Masazumi Matsumura, Sergei V. Chetyrkin, Peter S. Nelson, Elena A. Lapshina, Daniel W. Lin, Natalia Y. Kedishvili, Olga V. Belyaeva
Publikováno v:
Journal of Biological Chemistry. 277:28909-28915
All-trans-retinoic acid is a metabolite of vitamin A (all-trans-retinol) that functions as an activating ligand for a family of nuclear retinoic acid receptors. The intracellular levels of retinoic acid in tissues are tightly regulated, although the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84032cca39c9e3d4183224d2962b3f0e
https://doi.org/10.1074/jbc.m202588200
https://doi.org/10.1074/jbc.m202588200
Autor:
Saburo Suzuki, Masazumi Matsumura
Publikováno v:
The Journal of Japan Institute of Navigation. 100:75-80
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3334e9c79f5e6416c0c6eab4cfff01a5
https://doi.org/10.9749/jin.100.75
https://doi.org/10.9749/jin.100.75
Publikováno v:
The Journal of Japan Institute of Navigation. 98:395-402
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::02fab671e3890259bd78ce0129b5054d
https://doi.org/10.9749/jin.98.395
https://doi.org/10.9749/jin.98.395
Publikováno v:
Journal of pharmaceutical sciences. 102(6)
Human immunoglobulin G1 (IgG1) and immunoglobulin G2 (IgG2) antibodies contain multiple disulfide bonds, which are an integral part of the structure and stability of the protein. Open disulfide bonds have been detected in a number of therapeutic and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::915f8a99480ab5bf7289698f9d0843c1
https://pubmed.ncbi.nlm.nih.gov/23559428
https://pubmed.ncbi.nlm.nih.gov/23559428
Autor:
Masazumi Matsumura, Yutaka Saito, Per A. Peterson, Ian A. Wilson, Enrico A. Stura, Daved H. Fremont
Publikováno v:
Journal of Molecular Biology. 228:975-982
X-ray quality crystals of a soluble murine class I H-2Kb molecule complexed with three different peptide antigens were grown in several forms by streak seeding and macroseeding methods. Co-crystals with VSV-8 (RGYVYGQL), OVA-8 (SIINFEKL) and SEV-9 (F
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e62a12b37ec5bb1771c7caf3a9c1e83
https://doi.org/10.1016/0022-2836(92)90881-j
https://doi.org/10.1016/0022-2836(92)90881-j